JBC Oz Biosciences

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on May 3, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/19/17057    most recent
M111804200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nonato, M. C.
Right arrow Articles by Clardy, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nonato, M. C.
Right arrow Articles by Clardy, J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print February 21, 2002
J. Biol. Chem, 10.1074/jbc.M111804200
Submitted on December 11, 2001
Revised on February 19, 2002
Accepted on February 20, 2002

Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha

M. Cristina Nonato, Joanne Widom, and Jon Clardy

Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14850

Corresponding Author: mcn22{at}cornell.edu

Eukaryotic translation initiation factor 2alpha (eIF2alpha) is a member of the eIF2 heterotrimeric complex that binds and delivers Met-tRNAiMet to the 40S ribosomal subunit in a GTP-dependent manner. Phosphorylation/dephosphorylation of eIF2alpha at Ser51 is the major regulator of protein synthesis in eukaryotic cells. Here, we report the first structural analysis on eIF2: the three-dimensional structure of a 22 kDa N-terminal portion of human eIF2alpha by X-ray diffraction at 1.9 Å resolution. This structure contains two major domains. The N-terminus is a b-barrel with five antiparallel b-strands in an oligonucleotide binding domain (OB domain) fold. The phosphorylation site (Ser51) is on the loop connecting Beta3 and Beta4 in the OB domain. A helical domain follows the OB domain, and the first helix has extensive interactions, including a disulphide bridge, to firmly position it with respect to the OB domain. The two domains meet along a negatively charged groove with highly conserved residues, which suggests a role in protein-protein interaction.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
E. J. Seo, F. Liu, M. Kawagishi-Kobayashi, T. L. Ung, C. Cao, A. C. Dar, F. Sicheri, and T. E. Dever
Protein kinase PKR mutants resistant to the poxvirus pseudosubstrate K3L protein
PNAS, November 4, 2008; 105(44): 16894 - 16899.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
V. V. Zeenko, C. Wang, M. Majumder, A. A. Komar, M. D. Snider, W. C. Merrick, R. J. Kaufman, and M. Hatzoglou
An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation
RNA, March 1, 2008; 14(3): 593 - 602.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Dey, B. Trieselmann, E. G. Locke, J. Lu, C. Cao, A. C. Dar, T. Krishnamoorthy, J. Dong, F. Sicheri, and T. E. Dever
PKR and GCN2 Kinases and Guanine Nucleotide Exchange Factor Eukaryotic Translation Initiation Factor 2B (eIF2B) Recognize Overlapping Surfaces on eIF2{alpha}
Mol. Cell. Biol., April 15, 2005; 25(8): 3063 - 3075.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
B. S. Laursen, H. P. Sorensen, K. K. Mortensen, and H. U. Sperling-Petersen
Initiation of Protein Synthesis in Bacteria
Microbiol. Mol. Biol. Rev., March 1, 2005; 69(1): 101 - 123.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Yatime, E. Schmitt, S. Blanquet, and Y. Mechulam
Functional Molecular Mapping of Archaeal Translation Initiation Factor 2
J. Biol. Chem., April 16, 2004; 279(16): 15984 - 15993.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
M. Tahara, A. Ohsawa, S. Saito, and M. Kimura
In Vitro Phosphorylation of Initiation Factor 2{alpha} (aIF2{alpha}) from Hyperthermophilic Archaeon Pyrococcus horikoshii OT3
J. Biochem., April 1, 2004; 135(4): 479 - 485.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
W. P. Boomershine, C. A. McElroy, H.-Y. Tsai, R. C. Wilson, V. Gopalan, and M. P. Foster
Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P
PNAS, December 23, 2003; 100(26): 15398 - 15403.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
M. Yao, A. Ohsawa, S. Kikukawa, I. Tanaka, and M. Kimura
Crystal Structure of Hyperthermophilic Archaeal Initiation Factor 5A: A Homologue of Eukaryotic Initiation Factor 5A (eIF-5A)
J. Biochem., January 1, 2003; 133(1): 75 - 81.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.